Kinetic non-optimality and vibrational stability of proteins
Statistical Mechanics
2007-05-23 v1 Soft Condensed Matter
q-bio
Abstract
Scaling of folding times in Go models of proteins and of decoy structures with the Lennard-Jones potentials in the native contacts reveal %robust power law trends when studied under optimal folding conditions. The power law exponent depends on the type of native geometry. Its value indicates lack of kinetic optimality in the model proteins. In proteins, mechanical and thermodynamic stabilities are correlated.
Cite
@article{arxiv.cond-mat/0102316,
title = {Kinetic non-optimality and vibrational stability of proteins},
author = {Marek Cieplak and Trinh Xuan Hoang},
journal= {arXiv preprint arXiv:cond-mat/0102316},
year = {2007}
}
Comments
REVTex, Proteins: Function, Structure and Genetics - in press